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Raw X-ray diffraction data for Dactylis glomerata alpha amylase

X-Ray synchrotron diffraction data for Dactylis glomerata alpha amylase, crystallized in 0.2 M ammonium sulphate, 25% w/v PEG 3350, 0.1 M Bis-Tris buffer pH 5.5. The diffraction images were collected to the resolution of 2.1A at the BESSY II beamline 14.1 in Berlin at 100K using a Pilatus 6M detector. The data was recorded using X-ray wavelength 0.9184A with oscillation angle 0.5° and crystal-to-detector distances 470mm.

Publisher: RepOD

Publication year: 2020

Type of resource: Dataset

Area of study: Natural and mathematical sciences

License for files: CC0-1.0

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Authors

Author Affiliation
Imiolczyk, Barbara Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland
Jaskolski, Mariusz Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland

Cite this dataset as:

Imiolczyk, B.; Jaskolski, M. (2020) Raw X-ray diffraction data for Dactylis glomerata alpha amylase. RepOD. http://dx.doi.org/10.18150/repod.0656867

Publicly available in RepOD since: 2020-05-19 09:30 (CEST)

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